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Conserved domains on  [gi|308327893|gb|EFP16744|]
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hypothetical protein TMBG_03524 [Mycobacterium tuberculosis SUMu002]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

PubMed:  1409539|12369917

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
161-383 3.32e-15

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


:

Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 74.27  E-value: 3.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 161 HWRHRDGPRPTLCVIHGFMGSSYLLNGLFFSLpwyyRSGYDVLLYTLPFHGQRAEKFSPFSgfgyftsglsgfAEAMAQA 240
Cdd:COG0596   15 HYREAGPDGPPVVLLHGLPGSSYEWRPLIPAL----AAGYRVIAPDLRGHGRSDKPAGGYT------------LDDLADD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 241 VYDFrsivdyLRHIGVDRIALTGISLGGYTSALLASVE-SRLEAVIpncpvvmpakLFDEWFpanKLVKLGLRLTNISRD 319
Cdd:COG0596   79 LAAL------LDALGLERVVLVGHSMGGMVALELAARHpERVAGLV----------LVDEVL---AALAEPLRRPGLAPE 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308327893 320 ELIAGLAYHGPLNYRPLLPKDRR--MIITGLGDRMAPPEHAVTLWKQWDRCALHWFPGS-HLLHVSQ 383
Cdd:COG0596  140 ALAALLRALARTDLRERLARITVptLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAgHFPPLEQ 206
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
161-383 3.32e-15

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 74.27  E-value: 3.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 161 HWRHRDGPRPTLCVIHGFMGSSYLLNGLFFSLpwyyRSGYDVLLYTLPFHGQRAEKFSPFSgfgyftsglsgfAEAMAQA 240
Cdd:COG0596   15 HYREAGPDGPPVVLLHGLPGSSYEWRPLIPAL----AAGYRVIAPDLRGHGRSDKPAGGYT------------LDDLADD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 241 VYDFrsivdyLRHIGVDRIALTGISLGGYTSALLASVE-SRLEAVIpncpvvmpakLFDEWFpanKLVKLGLRLTNISRD 319
Cdd:COG0596   79 LAAL------LDALGLERVVLVGHSMGGMVALELAARHpERVAGLV----------LVDEVL---AALAEPLRRPGLAPE 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308327893 320 ELIAGLAYHGPLNYRPLLPKDRR--MIITGLGDRMAPPEHAVTLWKQWDRCALHWFPGS-HLLHVSQ 383
Cdd:COG0596  140 ALAALLRALARTDLRERLARITVptLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAgHFPPLEQ 206
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
170-341 1.71e-06

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 49.04  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893  170 PTLCVIHGFMGSSYLLNGLFFSLPwyyRSGYDVLLYTLPFHGQraekfSPFsgfgyftsglsgfaeAMAQAVYDFRSIVD 249
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALA---RDGFRVIALDLRGFGK-----SSR---------------PKAQDDYRTDDLAE 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893  250 YLR----HIGVDRIALTGISLGGYTSALLA-----------SVESRLEAVIPNCPVVMPAKLFDEWFPANKLVKLGLRLT 314
Cdd:pfam00561  58 DLEyileALGLEKVNLVGHSMGGLIALAYAakypdrvkalvLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLG 137
                         170       180
                  ....*....|....*....|....*..
gi 308327893  315 NISRDELIAGLAYHGPLNYRPLLPKDR 341
Cdd:pfam00561 138 RLVAKLLALLLLRLRLLKALPLLNKRF 164
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
161-383 3.32e-15

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 74.27  E-value: 3.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 161 HWRHRDGPRPTLCVIHGFMGSSYLLNGLFFSLpwyyRSGYDVLLYTLPFHGQRAEKFSPFSgfgyftsglsgfAEAMAQA 240
Cdd:COG0596   15 HYREAGPDGPPVVLLHGLPGSSYEWRPLIPAL----AAGYRVIAPDLRGHGRSDKPAGGYT------------LDDLADD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 241 VYDFrsivdyLRHIGVDRIALTGISLGGYTSALLASVE-SRLEAVIpncpvvmpakLFDEWFpanKLVKLGLRLTNISRD 319
Cdd:COG0596   79 LAAL------LDALGLERVVLVGHSMGGMVALELAARHpERVAGLV----------LVDEVL---AALAEPLRRPGLAPE 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308327893 320 ELIAGLAYHGPLNYRPLLPKDRR--MIITGLGDRMAPPEHAVTLWKQWDRCALHWFPGS-HLLHVSQ 383
Cdd:COG0596  140 ALAALLRALARTDLRERLARITVptLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAgHFPPLEQ 206
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
166-394 6.37e-15

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 73.51  E-value: 6.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 166 DGPRPTLCVIHGFMGSSYllNGLFFSLPWYYRSGYDVLLYTLPFHGQRAEKFSpfsgfgyftsglsgfaeamAQAVYDFR 245
Cdd:COG1506   20 GKKYPVVVYVHGGPGSRD--DSFLPLAQALASRGYAVLAPDYRGYGESAGDWG-------------------GDEVDDVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 246 SIVDYLR---HIGVDRIALTGISLGGYTSALLASVESRL-EAVIPNCPVVMPAKLFDEWFPANKLVKLGLrltnisrDEL 321
Cdd:COG1506   79 AAIDYLAarpYVDPDRIGIYGHSYGGYMALLAAARHPDRfKAAVALAGVSDLRSYYGTTREYTERLMGGP-------WED 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 322 IAGLAYHGPLNY-----RPLLpkdrrmIITGLGDRMAPPEHAVTLWKQWDR----CALHWFPG-SH-LLHVSQLDYLRRM 390
Cdd:COG1506  152 PEAYAARSPLAYadklkTPLL------LIHGEADDRVPPEQAERLYEALKKagkpVELLVYPGeGHgFSGAGAPDYLERI 225

                 ....
gi 308327893 391 TVFL 394
Cdd:COG1506  226 LDFL 229
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
144-380 9.47e-14

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 70.03  E-value: 9.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 144 MRQRWSALTANN--IVHAQHWRHRDGPRPTLCVIHGFMGSSYLLNGLffsLPWYYRSGYDVLLYTLPFHGQraekfspfs 221
Cdd:COG2267    1 MTRRLVTLPTRDglRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAEL---AEALAAAGYAVLAFDLRGHGR--------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 222 gfgyfTSGLSGFAEAMAQAVYDFRSIVDYLRHIGVDRIALTGISLGGYTSALLAS-VESRLEAVIPNCP-------VVMP 293
Cdd:COG2267   69 -----SDGPRGHVDSFDDYVDDLRAALDALRARPGLPVVLLGHSMGGLIALLYAArYPDRVAGLVLLAPayradplLGPS 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 294 AKLFDEWFPANKLVKLGLrltnisrdeliaglayhgplnyrPLLpkdrrmIITGLGDRMAPPEHAVTLWKQW-DRCALHW 372
Cdd:COG2267  144 ARWLRALRLAEALARIDV-----------------------PVL------VLHGGADRVVPPEAARRLAARLsPDVELVL 194

                 ....*....
gi 308327893 373 FPG-SHLLH 380
Cdd:COG2267  195 LPGaRHELL 203
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
137-395 7.21e-13

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 68.02  E-value: 7.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 137 FRAINPTMRQRWSALTANNI-VHAQHWR--HRDGPRPTLCVIHGFMG--SSYLLNGlffslPWYYRSGYDVLLYTLPFHG 211
Cdd:COG1073    2 FPPSDKVNKEDVTFKSRDGIkLAGDLYLpaGASKKYPAVVVAHGNGGvkEQRALYA-----QRLAELGFNVLAFDYRGYG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 212 QraekfSP--FSGFGYFtsglsgfaeamaqAVYDFRSIVDYLR-HIGVD--RIALTGISLGGYTSALLASVESRLEAVIP 286
Cdd:COG1073   77 E-----SEgePREEGSP-------------ERRDARAAVDYLRtLPGVDpeRIGLLGISLGGGYALNAAATDPRVKAVIL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 287 NCPVVMPAKLFDEWFPANKLVKLGLR--LTNISRDELIAGLAYhgPLNY-----RPLLpkdrrmIITGLGDRMAPPEHAV 359
Cdd:COG1073  139 DSPFTSLEDLAAQRAKEARGAYLPGVpyLPNVRLASLLNDEFD--PLAKiekisRPLL------FIHGEKDEAVPFYMSE 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 308327893 360 TLWKqwdRCA----LHWFPG-SH--LLHVSQLDYLRRMTVFLQ 395
Cdd:COG1073  211 DLYE---AAAepkeLLIVPGaGHvdLYDRPEEEYFDKLAEFFK 250
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
175-397 2.42e-10

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 60.34  E-value: 2.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 175 IHGFMGSSYLLNGLFfslPWYYRSGYDVLLYTLPFHGQRAEKFSPFSgfgyftsglsgfAEAMAQAVydfRSIVDYLRHi 254
Cdd:COG1647   21 LHGFTGSPAEMRPLA---EALAKAGYTVYAPRLPGHGTSPEDLLKTT------------WEDWLEDV---EEAYEILKA- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 255 GVDRIALTGISLGGYTSALLASVESRLEAVIPNCPVVMPAKLFDEWFPANKLVKLGLRLTNIS-RDELIAGLAYHG-PLN 332
Cdd:COG1647   82 GYDKVIVIGLSMGGLLALLLAARYPDVAGLVLLSPALKIDDPSAPLLPLLKYLARSLRGIGSDiEDPEVAEYAYDRtPLR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 333 -----------YRPLLPKDRR--MIITGLGDRMAPPEHAVTLWKQW--DRCALHWFPGS-HLLHVS-QLDYLRRMTV-FL 394
Cdd:COG1647  162 alaelqrlireVRRDLPKITAptLIIQSRKDEVVPPESARYIYERLgsPDKELVWLEDSgHVITLDkDREEVAEEILdFL 241

                 ...
gi 308327893 395 QGL 397
Cdd:COG1647  242 ERL 244
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
170-341 1.71e-06

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 49.04  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893  170 PTLCVIHGFMGSSYLLNGLFFSLPwyyRSGYDVLLYTLPFHGQraekfSPFsgfgyftsglsgfaeAMAQAVYDFRSIVD 249
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALA---RDGFRVIALDLRGFGK-----SSR---------------PKAQDDYRTDDLAE 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893  250 YLR----HIGVDRIALTGISLGGYTSALLA-----------SVESRLEAVIPNCPVVMPAKLFDEWFPANKLVKLGLRLT 314
Cdd:pfam00561  58 DLEyileALGLEKVNLVGHSMGGLIALAYAakypdrvkalvLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLG 137
                         170       180
                  ....*....|....*....|....*..
gi 308327893  315 NISRDELIAGLAYHGPLNYRPLLPKDR 341
Cdd:pfam00561 138 RLVAKLLALLLLRLRLLKALPLLNKRF 164
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
166-300 2.58e-06

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 48.04  E-value: 2.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 166 DGPRPTLCVIHGFMGSSYLLNGLffsLPWYYRSGYDVLLYTLPFHGQRAEkfSPFSGFGYFTsglsgfAEAMAQAVYDFR 245
Cdd:COG0412   26 GGPRPGVVVLHEIFGLNPHIRDV---ARRLAAAGYVVLAPDLYGRGGPGD--DPDEARALMG------ALDPELLAADLR 94
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 308327893 246 SIVDYLR---HIGVDRIALTGISLGGYTSALLASVESRLEAVIPNCPVVMPAKLFDEW 300
Cdd:COG0412   95 AALDWLKaqpEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGGLPADDLLDLA 152
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
165-289 3.92e-05

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 45.18  E-value: 3.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893 165 RDGPRPTLCVIHGFMGSSYLLNGLFFslpwYYRSGYDVLLytLPFHGQRAEK--------FSPFSGFGYFTSGLSGFAEA 236
Cdd:COG3458   78 GEGPLPAVVEFHGYGGGRGLPHEDLD----WAAAGYAVLV--MDTRGQGSSWgdtpdpggYSGGALPGYMTRGIDDPDTY 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 308327893 237 MAQAVYD--FRSiVDYLR-HIGVD--RIALTGISLGGYTSALLASVESRLEAVIPNCP 289
Cdd:COG3458  152 YYRRVYLdaVRA-VDALRsLPEVDgkRIGVTGGSQGGGLALAAAALDPRVKAAAADVP 208
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
222-395 4.41e-04

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 41.06  E-value: 4.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893  222 GFGYFTS---GLSGFAEAMAQAVY---------DFRSIVDYLR---HIGVDRIALTGISLGGYTSALLASVESRL-EAVI 285
Cdd:pfam00326  14 GYVVAIAngrGSGGYGEAFHDAGKgdlgqnefdDFIAAAEYLIeqgYTDPDRLAIWGGSYGGYLTGAALNQRPDLfKAAV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893  286 PNCPVV-------MPAKLFDEWF---PANKLVKLGlrltnisRDELIAGLAYHGPLNYRPLlpkdrrMIITGLGDRMAPP 355
Cdd:pfam00326  94 AHVPVVdwlaymsDTSLPFTERYmewGNPWDNEEG-------YDYLSPYSPADNVKVYPPL------LLIHGLLDDRVPP 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 308327893  356 EHAVTLWKQWDRCA----LHWFPGS-H--LLHVSQLDYLRRMTVFLQ 395
Cdd:pfam00326 161 WQSLKLVAALQRKGvpflLLIFPDEgHgiGKPRNKVEEYARELAFLL 207
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
168-275 4.33e-03

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 38.35  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308327893  168 PRPTLCVIHGFMGSSYLLNGLFFSLpwyYRSGYDVLLYTLPFHGQraekfspfsgfgyfTSGLSGFAEAMAQAVYDFRSI 247
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADAL---AAQGFAVYAYDHRGHGR--------------SDGKRGHVPSFDDYVDDLDTF 65
                          90       100       110
                  ....*....|....*....|....*....|
gi 308327893  248 VDYL--RHIGVDRIALtGISLGGYTSALLA 275
Cdd:pfam12146  66 VDKIreEHPGLPLFLL-GHSMGGLIAALYA 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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